Ontology highlight
ABSTRACT:
SUBMITTER: Nguyen PH
PROVIDER: S-EPMC8836097 | biostudies-literature | 2021 Feb
REPOSITORIES: biostudies-literature
Nguyen Phuong H PH Ramamoorthy Ayyalusamy A Sahoo Bikash R BR Zheng Jie J Faller Peter P Straub John E JE Dominguez Laura L Shea Joan-Emma JE Dokholyan Nikolay V NV De Simone Alfonso A Ma Buyong B Nussinov Ruth R Najafi Saeed S Ngo Son Tung ST Loquet Antoine A Chiricotto Mara M Ganguly Pritam P McCarty James J Li Mai Suan MS Hall Carol C Wang Yiming Y Miller Yifat Y Melchionna Simone S Habenstein Birgit B Timr Stepan S Chen Jiaxing J Hnath Brianna B Strodel Birgit B Kayed Rakez R Lesné Sylvain S Wei Guanghong G Sterpone Fabio F Doig Andrew J AJ Derreumaux Philippe P
Chemical reviews 20210205 4
Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting either the central nervous system or a variety of peripheral tissues. Structural and dynamic characterization of all species along the pathways from monomers to fibrils is challenging by experimental and computational means because they involve intrinsically disordered proteins in most diseases. Yet understanding how amyloid species become toxic is the challenge in developing a treatment for these diseases. H ...[more]